PCL8_YEAST
ID PCL8_YEAST Reviewed; 492 AA.
AC Q08966; D6W3F1; Q6B153;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=PHO85 cyclin-8;
GN Name=PCL8; OrderedLocusNames=YPL219W; ORFNames=P1745;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INTERACTION WITH PHO85.
RX PubMed=9032248; DOI=10.1128/mcb.17.3.1212;
RA Measday V., Moore L., Retnakaran R., Lee J., Donoviel M., Neiman A.M.,
RA Andrews B.J.;
RT "A family of cyclin-like proteins that interact with the Pho85 cyclin-
RT dependent kinase.";
RL Mol. Cell. Biol. 17:1212-1223(1997).
RN [5]
RP FUNCTION.
RX PubMed=9584169; DOI=10.1128/mcb.18.6.3289;
RA Huang D., Moffat J., Wilson W.A., Moore L., Cheng C., Roach P.J.,
RA Andrews B.J.;
RT "Cyclin partners determine Pho85 protein kinase substrate specificity in
RT vitro and in vivo: control of glycogen biosynthesis by Pcl8 and Pcl10.";
RL Mol. Cell. Biol. 18:3289-3299(1998).
RN [6]
RP FUNCTION.
RX PubMed=12407105; DOI=10.1074/jbc.m208058200;
RA Tan Y.S.H., Morcos P.A., Cannon J.F.;
RT "Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 in
RT vivo.";
RL J. Biol. Chem. 278:147-153(2003).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Cyclin partner of the cyclin-dependent kinase (CDK) PHO85.
CC Together with cyclin PCL10, negatively controls glycogen accumulation
CC under favorable growth conditions. Involved in phosphorylation and
CC negative regulation of glycogen synthase GSY2. Also has minor GLC8
CC kinase activity. {ECO:0000269|PubMed:12407105,
CC ECO:0000269|PubMed:9584169}.
CC -!- SUBUNIT: Forms a cyclin-CDK complex with PHO85.
CC -!- INTERACTION:
CC Q08966; P17157: PHO85; NbExp=8; IntAct=EBI-37056, EBI-13327;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. PHO80 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z73575; CAA97934.1; -; Genomic_DNA.
DR EMBL; AY693227; AAT93246.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11217.1; -; Genomic_DNA.
DR PIR; S65238; S65238.
DR RefSeq; NP_015105.1; NM_001184033.1.
DR AlphaFoldDB; Q08966; -.
DR SMR; Q08966; -.
DR BioGRID; 35966; 150.
DR ComplexPortal; CPX-1691; PCL8-PHO85 kinase complex.
DR DIP; DIP-1509N; -.
DR IntAct; Q08966; 6.
DR MINT; Q08966; -.
DR STRING; 4932.YPL219W; -.
DR iPTMnet; Q08966; -.
DR MaxQB; Q08966; -.
DR PaxDb; Q08966; -.
DR PRIDE; Q08966; -.
DR EnsemblFungi; YPL219W_mRNA; YPL219W; YPL219W.
DR GeneID; 855882; -.
DR KEGG; sce:YPL219W; -.
DR SGD; S000006140; PCL8.
DR VEuPathDB; FungiDB:YPL219W; -.
DR eggNOG; KOG1674; Eukaryota.
DR GeneTree; ENSGT00390000000862; -.
DR HOGENOM; CLU_043984_0_0_1; -.
DR InParanoid; Q08966; -.
DR OMA; RIQSKCM; -.
DR BioCyc; YEAST:G3O-34108-MON; -.
DR PRO; PR:Q08966; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08966; protein.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; ISS:SGD.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0005977; P:glycogen metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IMP:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0005979; P:regulation of glycogen biosynthetic process; IC:ComplexPortal.
DR InterPro; IPR013922; Cyclin_PHO80-like.
DR PANTHER; PTHR15615; PTHR15615; 1.
DR Pfam; PF08613; Cyclin; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cyclin; Cytoplasm; Glycogen metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..492
FT /note="PHO85 cyclin-8"
FT /id="PRO_0000271787"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 234
FT /note="N -> T (in Ref. 3; AAT93246)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 55431 MW; 1C0E7B8F126DC4CC CRC64;
MANDQDPNKS LINDALTRSM SEFYDDDDDN DSDMCRANDE GEDVFDLPLK VGVSQSRNFS
EVNDVLDPLS SLHGPSKKVR FEQQKQQQQH QQLHNDFNTD FNLKSPSSKK MGVEQLIQSA
NEINDYLANN IDKVNSFNSE LLSGSGKLPG RVKSDTATQG TGRLDSMSNF ALSDTELDND
DDNYLLDPLA NASSTTPTVE HHGYSLLDKA LSTSDKEKIY TNKVNSNSQI DTDNHSHESG
NTTNNETDEN ESSEILDYTK FDSFPYPPSS APNGEPPDLK VLSIECEQEN EKELRRISLL
LDHYESIPKI PELSDDEALS KFRENIELIL QLSKKINDNA NTLAISSEDP QKFVNFVMKN
PPSLSFRDFI DRIQNKCMFG AVVYLGATYL LQLVFLTRDE MDGPIKLKAK LQEDQAHRII
ISTIRIATKL LEDFVHSQNY ICKVFGISKR LLTKLEISFM ASVNFDGLMI TCEKLEKTLH
ILDDTRQALG NT
